ID A0A0L8IDH7_OCTBM Unreviewed; 1264 AA.
AC A0A0L8IDH7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Tripeptidyl-peptidase 2 {ECO:0000256|ARBA:ARBA00020244};
DE EC=3.4.14.10 {ECO:0000256|ARBA:ARBA00012462};
DE AltName: Full=Tripeptidyl aminopeptidase {ECO:0000256|ARBA:ARBA00032232};
GN ORFNames=OCBIM_22020590mg {ECO:0000313|EMBL:KOF99075.1};
OS Octopus bimaculoides (California two-spotted octopus).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC Coleoidea; Octopodiformes; Octopoda; Incirrata; Octopodidae; Octopus.
OX NCBI_TaxID=37653 {ECO:0000313|EMBL:KOF99075.1};
RN [1] {ECO:0000313|EMBL:KOF99075.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=UCB-OBI-ISO-001 {ECO:0000313|EMBL:KOF99075.1};
RC TISSUE=Gonad {ECO:0000313|EMBL:KOF99075.1};
RA Tran T., Druce J.;
RT "MeaNS - Measles Nucleotide Surveillance Program.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal tripeptide from a polypeptide.;
CC EC=3.4.14.10; Evidence={ECO:0000256|ARBA:ARBA00001910};
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240}.
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DR EMBL; KQ416030; KOF99075.1; -; Genomic_DNA.
DR RefSeq; XP_014778070.1; XM_014922584.1.
DR AlphaFoldDB; A0A0L8IDH7; -.
DR STRING; 37653.A0A0L8IDH7; -.
DR EnsemblMetazoa; Ocbimv22020590m; Ocbimv22020590m.p; Ocbimv22020590m.g.
DR EnsemblMetazoa; XM_014922584.1; XP_014778070.1; LOC106874742.
DR GeneID; 106874742; -.
DR KEGG; obi:106874742; -.
DR OMA; SLRDFQC; -.
DR OrthoDB; 2441948at2759; -.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd04857; Peptidases_S8_Tripeptidyl_Aminopeptidase_II; 1.
DR Gene3D; 1.25.40.710; -; 1.
DR Gene3D; 2.20.25.690; -; 1.
DR Gene3D; 2.60.40.3170; -; 1.
DR Gene3D; 6.10.250.3080; -; 1.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR InterPro; IPR034051; TPP_II_domain.
DR InterPro; IPR022232; TPPII_C_art.
DR InterPro; IPR046939; TPPII_C_sf.
DR InterPro; IPR048384; TPPII_GBD.
DR InterPro; IPR048383; TPPII_Ig-like-1.
DR InterPro; IPR022229; TPPII_Ig-like-2.
DR InterPro; IPR046940; TPPII_Ig-like_sf.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR PANTHER; PTHR43806:SF14; TRIPEPTIDYL-PEPTIDASE 2; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR Pfam; PF12580; TPPII; 1.
DR Pfam; PF12583; TPPII_C; 1.
DR Pfam; PF21316; TPPII_GBD; 1.
DR Pfam; PF21223; TPPII_Ig-like-1; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 34..486
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT DOMAIN 521..635
FT /note="Tripeptidyl-peptidase II first Ig-like"
FT /evidence="ECO:0000259|Pfam:PF21223"
FT DOMAIN 655..743
FT /note="Tripeptidyl-peptidase II galactose-binding"
FT /evidence="ECO:0000259|Pfam:PF21316"
FT DOMAIN 779..965
FT /note="Tripeptidyl peptidase II second Ig-like"
FT /evidence="ECO:0000259|Pfam:PF12580"
FT DOMAIN 1010..1076
FT /note="Tripeptidyl peptidase II C-terminal"
FT /evidence="ECO:0000259|Pfam:PF12583"
FT ACT_SITE 43
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 263
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 448
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 1264 AA; 141408 MW; D93D0CCBAF65BA20 CRC64;
MASSADTVFP VEGLLPKKET GSTSFLAKYP DYDGRGILIA VLDTGVDPGA AGLQVTSDDK
PKILDLIDTT GSGDVDTSTV VEVNQNEIIG LTGRNLKIPE SWNNPTGQYY IGIKNAYDLY
PKTLKERISK ERTDRLWSPP HRLALAEVTR KLEEFDTSHP YPNPDELNIR EDLTNQIEIL
NNLDKKHNDC GPVFDCVVFH DGETWRACVD TSEKGQLDQC ELLASYREER KFARLSYADM
LNFSVNIHNN GTLLEIVTNA GSHGTHVGCI AAGYFPETPE RNGVAPGAQI ISIKIGDTRL
KSMETGSALV RAMVKVIEYK CDLVNYSYGE AAHWVNGGRV CDILSEVVNK HGVIFVSSAG
NNGPALSTVG VPGGTTTSMI GVGACVCPSM MVAEYSLRER LPIMQYPWSS RGPAPDGFMG
VCISAPGGAI ASVPNWTLKG CQLMNGTSMS SPNACGCIAL ILSGLKANSI PYSPFSVRRA
LMNAAQPIEG CEPFGLGAGL LQVEKAYDFL TNFSEAKERN VQFLVTVPGG NRGIYIRDIC
KLNKINEISV SVELSYLENK TVQEDKIDFN LQLCLTCDAS WVEIPSHLEL NTFRSIGVQV
DPRGLPHGAH YTEIKAFDVS CLAKGPVFTV PITVIVPIKI TDDVHHTVSF TDVKFKPGQI
KRHFIHVPEG ATFGVLKIES KDTEKSCRFL LHTLQLLPQC QYRKHEFDKL VTLSDQGEFV
QSFPVLDSNI LEVCLAKWWA NLGEVTLDYS VTFRGISVDS KQIVMHAADG IARCNVKATL
RHEEICPSVC LKSLAQPLRP AEHKLRSLNG PRDLLPEGRQ IYAIELTYNF HLSKGEEVTP
DCSLLSDLLY ESEYESQLWM LFDSNKYFIS AGDAYPTRYS VKLEKGDYVI LLQIRHDNRE
MVEKLKDTVL VLHHRLQNAL FLDIHACWQN TLSPQAKKLC SLCAHKGTTY PLFFCPLPDD
KLPKSHGPGN YLTGSLFVLK DEPLKKSTSV PFKYILTELV KKPKNSNGKN KESKEKTAEE
EYEEALRDLK ISWLTKLDDC DNLYKELSTE YQDYLLLHVA RLQALDADKD RMKKLPEITK
VAEHILSNID KDALLAYYGM KSDPRPNSSS IKIEMDKQKN ILIDTFVKLG CAQADTHLEA
MKPLNAVTSG DDEQVTGVED DEDNDCEHVI PKVPIQEIDS IFEELIKWVD PFDSKVIEFS
VRHAMMHKLY GRSLRFLLKQ NEEKPSKQQE KRCTEIFKQL NWNHCAEYFE NLLLVKYPKS
YRPF
//
